(data stored in SCRATCH zone)

SWISSPROT: C5DD78_LACTC

ID   C5DD78_LACTC            Unreviewed;       492 AA.
AC   C5DD78;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=RNA helicase {ECO:0000256|SAAS:SAAS00892872};
DE            EC=3.6.4.13 {ECO:0000256|SAAS:SAAS00892872};
GN   OrderedLocusNames=KLTH0B08998g {ECO:0000313|EMBL:CAR21739.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21739.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21739.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|SAAS:SAAS01117681};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492, ECO:0000256|SAAS:SAAS00892877}.
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DR   EMBL; CU928166; CAR21739.1; -; Genomic_DNA.
DR   RefSeq; XP_002552177.1; XM_002552131.1.
DR   STRING; 381046.XP_002552177.1; -.
DR   EnsemblFungi; CAR21739; CAR21739; KLTH0B08998g.
DR   GeneID; 8291020; -.
DR   KEGG; lth:KLTH0B08998g; -.
DR   HOGENOM; HOG000268799; -.
DR   InParanoid; C5DD78; -.
DR   KO; K13179; -.
DR   OMA; MAHHSQT; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   CDD; cd00079; HELICc; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DD78.
DR   SWISS-2DPAGE; C5DD78.
KW   ATP-binding {ECO:0000256|RuleBase:RU000492,
KW   ECO:0000256|SAAS:SAAS00892855};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Helicase {ECO:0000256|RuleBase:RU000492,
KW   ECO:0000256|SAAS:SAAS00892858};
KW   Hydrolase {ECO:0000256|RuleBase:RU000492,
KW   ECO:0000256|SAAS:SAAS00892861};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000492,
KW   ECO:0000256|SAAS:SAAS00892867};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   RNA-binding {ECO:0000256|SAAS:SAAS00892852}.
FT   DOMAIN       28     56       Q_MOTIF. {ECO:0000259|PROSITE:PS51195}.
FT   DOMAIN       59    235       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      249    419       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   MOTIF        28     56       Q motif. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00552}.
SQ   SEQUENCE   492 AA;  55097 MW;  D196BD110F94EA88 CRC64;
     MGEVEEKAHS KKRSADAVEA SENDGYKEKF AELNLSPPTM KAIDKMGFTT MTQVQSRTIP
     PLLAGRDVLG AAKTGSGKTL AFLLPAIEML HSLKFKPRNG TGVIVITPTR ELALQIFGVA
     KTLMEFHSQT FGIVIGGANR RQEADKLAKG VNLLIATPGR LLDHLQNTKD FVFKNLKALV
     IDEADRILEI GFEDEMRQIV KILPSEERQT MLFSATQTTK VEDLARISLR PGPLFINVDS
     EKQTSTADGL EQGYVVCDSD KRFLLLFSFL KRNQKKKIIV FLSSCNSVRY YAELLNYIDL
     PVLELHGKQK QQKRTNTFFE FCNAERGTLV CTDVAARGLD IPAVDWIIQF DPPDDPRDYI
     HRVGRTARGS KGKGKSLMFL TPNELGFLRY LKAAKVPLNE YEFPSNKIAN VQSQLEKLIK
     SNYHLHQIAK DGYRSYLQAY SSHSLKTVYQ IDKLDLAKVA KSYGFPIPPK VNITIGASGK
     TPPSKKRKPS RN
//

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